Structure of PDB 1jee Chain A

Receptor sequence
>1jeeA (length=510) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PAPHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNG
GFSPLTGFLNENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTR
IALFQDDEIPIAILTVQDVYKPNKTIEAEKVFRGDPEHPAISYLFNVAGD
YYVGGSLEAIQLPQHYDYPGLRKTPAQLRLEFQSRQWDRVVAFQTRNPMH
RAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPN
GIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSKG
VDFYGPYDAQELVESYKHELDIEVVPFRMVTYLPDEDRYAPIDQIDTTKT
RTLNISGTELRRRLRVGGEIPEWFSYPEVVKILRESNPPRPKQGFSIVLG
NSLTVSREQLSIALLSTFLQFGGGRYYKIFEHNNKTELLSLIQDFIGSGS
GLIIPNQWEDDKDSVVGKQNVYLLDTSSSADIQLESADEPISHIVQKVVL
FLEDNGFFVF
3D structure
PDB1jee The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T196 R197 H201 H204 R290
Catalytic site (residue number reindexed from 1) T195 R196 H200 H203 R289
Enzyme Commision number 2.7.7.4: sulfate adenylyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A E46 P164 H166 E45 P163 H165
BS02 LCO A P199 H201 L361 P198 H200 L360
BS03 POP A H204 N355 I356 H203 N354 I355
BS04 ADX A F194 Q195 T196 R197 N198 H204 L207 G289 R290 H292 A293 R329 M330 V331 F193 Q194 T195 R196 N197 H203 L206 G288 R289 H291 A292 R328 M329 V330
Gene Ontology
Molecular Function
GO:0004781 sulfate adenylyltransferase (ATP) activity
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0000096 sulfur amino acid metabolic process
GO:0000103 sulfate assimilation
GO:0006790 sulfur compound metabolic process
GO:0010134 sulfate assimilation via adenylyl sulfate reduction
GO:0019379 sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
GO:0070814 hydrogen sulfide biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jee, PDBe:1jee, PDBj:1jee
PDBsum1jee
PubMed11700067
UniProtP08536|MET3_YEAST Sulfate adenylyltransferase (Gene Name=MET3)

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